The statement 'interactions of the hydrophobic and hydrophilic amino acids help to anchor the protein in the membrane' explains why protein folding is critical. This process is fundamental for the function of transmembrane proteins.
Protein folding refers to the process by which a polypeptide (i.e., a protein) adopts its final tridimensional 3D shape (conformation).
In a protein, some amino acids contain hydrophilic R groups, whereas other amino acids contain hydrophobic R groups.
During protein folding, hydrophobic amino acids are arranged so they can interact with the long chains of the fatty acids in the internal region of the lipid bilayer, whereas hydrophilic amino acids are arranged so they interact with water on the surface of the cell membrane.
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